EC Number   |
Inhibitors |
Structure  |
|---|
   3.4.24.11 | more |
proteins derived from the Tat protein of HIV |
 |
| 3.4.24.11 | more |
both staurosporine-stimulated caspase-3 activation, p53 and neprilysin expression and activity are not affected by over-expression or depletion of presenilin complex component TMP21 |
|
| 3.4.24.11 | more |
application of aldosterone, atrial natriuretic peptide, asymmetric dimethylarginine, and angiotensin peptides fail to cause down-regulation of renal neprilysin expression in vitro |
|
| 3.4.24.11 | more |
no inhibition by 4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione and 4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione |
|
| 3.4.24.11 | more |
desing of neprilysin inhibitors containing an alpha-mercaptoketone HSC(R1R2)CO group, as zinc ligand, substituted alpha-mercaptoketones are specific neprilysin inhibitors, optimization of the enzyme-inhibitor interactions within the S1 subsite, overview. Role of the size of the inhibitor which interacts with the S1, S1', or S2' domain of the enzyme and the nature of the substituents R1, and R2 of the mercaptoketone group in inhibitor potency. Introduction of a cyclohexyl chain in R1, R2 position and a (3-thiophen)benzyl group in position R3 yields to the most potent inhibitor of this series with a Ki value |
|
| 3.4.24.11 | more |
structure-activity relationship studies. No or poor inhibition by 4-(2-aminoethyl)benzylsulfonyl fluoride (AEBSF), and Nalpha-tosyl-l-lysyl chloromethylketone (TLCK), and iodoacetamide |
|
| 3.4.24.11 | more |
molecular docking studies, overview. For substrate and inhibitor binding, Arg664 and Zn697 are identified as the most conserved residues |
|
| 3.4.24.11 | phosphate |
- |
  |
| 3.4.24.11 | EDTA |
- |
|
| 3.4.24.11 | EDTA |
complete inhibition |
|
